4P5D
CRYSTAL STRUCTURE OF RAT DNPH1 (RCL) WITH 6-NAPHTHYL-PURINE-RIBOSIDE-MONOPHOSPHATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
A | 0070694 | molecular_function | 5-hydroxymethyl-dUMP N-hydrolase activity |
C | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
C | 0070694 | molecular_function | 5-hydroxymethyl-dUMP N-hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue N6P C 201 |
Chain | Residue |
C | TYR13 |
C | ALA58 |
C | ILE65 |
C | ASN69 |
C | SER87 |
C | GLY89 |
C | GLU93 |
C | SER117 |
C | MET119 |
C | HOH304 |
C | HOH306 |
C | CYS15 |
C | HOH330 |
C | HOH344 |
C | GLY16 |
C | SER17 |
C | ILE18 |
C | ARG19 |
C | GLY20 |
C | HIS45 |
C | GLU57 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue N6P A 201 |
Chain | Residue |
A | TYR13 |
A | CYS15 |
A | GLY16 |
A | SER17 |
A | ILE18 |
A | ARG19 |
A | GLY20 |
A | HIS45 |
A | VAL46 |
A | GLU57 |
A | ALA58 |
A | ILE65 |
A | ASN69 |
A | SER87 |
A | GLY89 |
A | VAL90 |
A | GLU93 |
A | SER117 |
A | MET119 |
A | HOH305 |
A | HOH315 |
A | HOH369 |
A | HOH385 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | ARG34 |
A | ARG36 |
A | ARG37 |
A | HOH304 |
A | HOH317 |
A | HOH382 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23385460, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359, ECO:0007744|PDB:4FYH, ECO:0007744|PDB:4FYI, ECO:0007744|PDB:4FYK, ECO:0007744|PDB:4KXL, ECO:0007744|PDB:4KXM, ECO:0007744|PDB:4KXN, ECO:0007744|PDB:4P5D |
Chain | Residue | Details |
C | GLY16 | |
A | ARG19 | |
A | GLY20 | |
A | SER87 | |
A | GLY89 | |
A | GLU93 | |
C | ILE18 | |
C | ARG19 | |
C | GLY20 | |
C | SER87 | |
C | GLY89 | |
C | GLU93 | |
A | GLY16 | |
A | ILE18 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: in other chain => ECO:0000269|PubMed:23385460, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359, ECO:0007744|PDB:4FYH, ECO:0007744|PDB:4FYI, ECO:0007744|PDB:4FYK, ECO:0007744|PDB:4KXL, ECO:0007744|PDB:4KXM, ECO:0007744|PDB:4KXN, ECO:0007744|PDB:4P5D |
Chain | Residue | Details |
C | SER117 | |
A | SER117 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O43598 |
Chain | Residue | Details |
C | SER17 | |
C | SER87 | |
C | SER112 | |
C | SER127 | |
A | SER17 | |
A | SER87 | |
A | SER112 | |
A | SER127 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
C | SER117 | |
A | SER117 |